Arányi P
J Recept Res. 1984;4(1-6):385-96. doi: 10.3109/10799898409042563.
Activation and deactivation of the chick thymus glucocorticoid receptor protein was studied in ordinary and heavy water by DNA-cellulose binding of the tritiated triamcinolone acetonide-receptor complex. Activation was significantly slower in heavy water if it was promoted by incubation at elevated temperature in buffers of low ionic strength. In the presence of 300 mM KC1 or after separation from the low molecular weight cytosol constituents, the complex was activated at the same rate in both solvents. Deactivation (time dependent loss of DNA-binding capacity) was much faster in ordinary than in heavy water regardless of gel filtration or the presence of KC1. A model of receptor activation-deactivation was constructed on the basis of these data that accounts for the observed kinetic deuterium isotope effects and reveals some submolecular details of the process.
通过氚化曲安奈德-受体复合物的DNA-纤维素结合，在普通水和重水中研究了鸡胸腺糖皮质激素受体蛋白的激活和失活。如果在低离子强度缓冲液中于升高的温度下孵育来促进激活，重水中的激活明显更慢。在存在300 mM KCl的情况下或从低分子量胞质溶胶成分中分离后，该复合物在两种溶剂中的激活速率相同。无论凝胶过滤或KCl的存在如何，失活（DNA结合能力的时间依赖性丧失）在普通水中比重水中快得多。基于这些数据构建了受体激活-失活模型，该模型解释了观察到的动力学氘同位素效应，并揭示了该过程的一些亚分子细节。
